EzCatDB: D00464

DB codeD00464
RLCP classification3.1107.6300.74
CATH domainDomain 12.160.10.10Catalytic domain
Domain 21.20.1180.10
E.C.2.3.1.129
CSA1lxa
MACiEM0069

CATH domainRelated DB codes (homologues)
2.160.10.10S00167,D00094,D00417

Enzyme Name
Swiss-protKEGG

P0A722O25927
Protein nameAcyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferaseAcyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferaseacyl-[acyl-carrier-protein]---UDP-N-acetylglucosamineO-acyltransferase
UDP-N-acetylglucosamine acyltransferase
uridine diphosphoacetylglucosamine acyltransferase
acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamineO-acyltransferase
(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3-hydroxytetradecanoyl)transferase
SynonymsUDP-N-acetylglucosamine acyltransferase
EC 2.3.1.129
UDP-N-acetylglucosamine acyltransferase
EC 2.3.1.129

KEGG pathways
MAP codePathways
MAP00540Lipopolysaccharide biosynthesis

Swiss-prot:Accession NumberP0A722O25927
Entry nameLPXA_ECOLILPXA_HELPY
Activity(R)-3-hydroxytetradecanoyl-[acyl-carrier- protein] + UDP-N-acetylglucosamine = [acyl-carrier-protein] + UDP- 3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine.(R)-3-hydroxytetradecanoyl-[acyl-carrier- protein] + UDP-N-acetylglucosamine = [acyl-carrier-protein] + UDP- 3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine.
SubunitHomotrimer.Homotrimer (By similarity).
Subcellular locationCytoplasm.Cytoplasm (By similarity).
Cofactor



SubstratesProducts
KEGG-idC04688C00043C00229C04738
Compound(R)-3-Hydroxytetradecanoyl-[acyl-carrier protein]UDP-N-acetylglucosamineAcyl-carrier proteinUDP-3-O-(3-hydroxytetradecanoyl)-N-acetylglucosamine
Typecarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide groupamide group,carbohydrate,nucleotidecarbohydrate,peptide/protein,phosphate group/phosphate ion,sulfhydryl groupamide group,carbohydrate,lipid,nucleotide
1lxaA01UnboundUnboundUnboundUnbound
1j2zA01UnboundAnalogue:SOGUnboundUnbound
1lxaA02UnboundUnboundUnboundUnbound
1j2zA02UnboundUnboundUnboundUnbound

Active-site residues
resource
literature [8]
pdbCatalytic residues
1lxaA01HIS 125
1j2zA01HIS 121
1lxaA02
1j2zA02

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]FIG. 6, p.27054
[11]p.774
[12]p.1385-1386

references
[1]
PubMed ID2180947
JournalJ Biol Chem
Year1990
Volume265
Pages6394-402
AuthorsGalloway SM, Raetz CR
TitleA mutant of Escherichia coli defective in the first step of endotoxin biosynthesis
[2]
PubMed ID8293817
JournalFEBS Lett
Year1994
Volume337
Pages289-92
AuthorsVuorio R, Harkonen T, Tolvanen M, Vaara M
TitleThe novel hexapeptide motif found in the acyltransferases LpxA and LpxD of lipid A biosynthesis is conserved in various bacteria.
[3]
PubMed ID7567967
JournalProteins
Year1995
Volume22
Pages191-2
AuthorsPfitzner U, Raetz CR, Roderick SL
TitleCrystallization of UDP-N-acetylglucosamine O-acyltransferase from Escherichia coli
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID96069822
PubMed ID7481807
JournalScience
Year1995
Volume270
Pages997-1000
AuthorsRaetz CR, Roderick SL
TitleA left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase
Related PDB1lxa
Related Swiss-protP0A722
[5]
PubMed ID9242624
JournalJ Biol Chem
Year1997
Volume272
Pages19688-96
AuthorsOdegaard TJ, Kaltashov IA, Cotter RJ, Steeghs L, van der Ley P, Khan S, Maskell DJ, Raetz CR
TitleShortened hydroxyacyl chains on lipid A of Escherichia coli cells expressing a foreign UDP-N-acetylglucosamine O-acyltransferase
[6]
PubMed ID9829962
JournalJ Biol Chem
Year1998
Volume273
Pages32369-72
AuthorsWyckoff TJ, Lin S, Cotter RJ, Dotson GD, Raetz CR
TitleHydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases.
[7]
PubMed ID9575543
JournalProg Clin Biol Res
Year1998
Volume397
Pages1-14
AuthorsRaetz CR
TitleEnzymes of lipid A biosynthesis
[8]
PubMed ID10480918
JournalJ Biol Chem
Year1999
Volume274
Pages27047-55
AuthorsWyckoff TJ, Raetz CR
TitleThe active site of Escherichia coli UDP-N-acetylglucosamine acyltransferase. Chemical modification and site-directed mutagenesis
[9]
PubMed ID10653812
JournalBiophys J
Year2000
Volume78
Pages994-1000
AuthorsKhurana R, Fink AL
TitleDo parallel beta-helix proteins have a unique fourier transform infrared spectrum?
[10]
PubMed ID11976505
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages864-6
AuthorsLee BI, Lee JY, Moon J, Han BW, Suh SW
TitleCrystallization and preliminary X-ray crystallographic analysis of UDP-N-acetylglucosamine acyltransferase from Helicobacter pylori.
[11]
PubMed ID14579368
JournalProteins
Year2003
Volume53
Pages772-4
AuthorsLee BI, Suh SW
TitleCrystal structure of UDP-N-acetylglucosamine acyltransferase from Helicobacter pylori.
[12]
PubMed ID15491619
JournalJ Mol Biol
Year2004
Volume343
Pages1379-89
AuthorsJain NU, Wyckoff TJ, Raetz CR, Prestegard JH
TitleRapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein.

comments
According to the literature [8], [11] & [12], the reaction proceeds as follows:
(1) His125 (of 1lxa) acts as a general base, which activates the acceptor group, 3-OH of UDP-GlcNAc substrate, by abstracting a proton from the group.
(2) The activated hydroxyl group makes a nucleophilic attack on the transferred acyl group.

createdupdated
2003-11-072012-06-04


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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